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Biophys. J. BioFAST: First Published August 19, 2005. doi:10.1529/biophysj.105.067330
© 2005 by the Biophysical Society.

A more recent version of this article appeared on November 1, 2005.
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BIOPHYSICAL THEORY AND MODELING

Protein Folding, Stability and Solvation Structure in Osmolyte Solutions

Jörg Rösgen 1*, Montgomery Pettitt 2 and David Wayne Bolen 1

1 Univ. of Texas Medical Branch
2 University of Houston

* To whom correspondence should be addressed. E-mail: jorosgen{at}utmb.edu.

Submitted on May 25, 2005
Revised on July 13, 2005
Accepted on 8 August 2005


  Abstract
An understanding of the impact of the crowded conditions in the cytoplasm on its biomolecules is of clear importance to biochemical, medical and pharmaceutical science. Our previous work on the use of small biochemical compounds to crowd protein solutions indicates that a quantitative description of their non-ideal behavior is possible and straightforward. Here, we show the structural origin of the non-ideal solution behavior. We discuss the consequences of these findings regarding protein folding stability and solvation in crowded solutions through a structural analysis of the m-value or the change in free energy difference of a macromolecule in solution with respect to the concentration of a third component.

Key Words: Chemical Potential, Hydration, Kirkwood-Buff Theory, Preferential Interaction, Protein Folding, Solvation




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Copyright © 2005 by the Biophysical Society.